PUR7_MYCLE
ID PUR7_MYCLE Reviewed; 297 AA.
AC O08361;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 25-MAY-2022, entry version 118.
DE RecName: Full=Phosphoribosylaminoimidazole-succinocarboxamide synthase;
DE EC=6.3.2.6;
DE AltName: Full=SAICAR synthetase;
GN Name=purC; OrderedLocusNames=ML2227; ORFNames=MLCB5.16;
OS Mycobacterium leprae (strain TN).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=272631;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TN;
RX PubMed=11234002; DOI=10.1038/35059006;
RA Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA Barrell B.G.;
RT "Massive gene decay in the leprosy bacillus.";
RL Nature 409:1007-1011(2001).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + ATP +
CC L-aspartate = (2S)-2-[5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-
CC 4-carboxamido]succinate + ADP + 2 H(+) + phosphate;
CC Xref=Rhea:RHEA:22628, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58443,
CC ChEBI:CHEBI:77657, ChEBI:CHEBI:456216; EC=6.3.2.6;
CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; 5-
CC amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-
CC phospho-D-ribosyl)imidazole-4-carboxylate: step 1/2.
CC -!- SIMILARITY: Belongs to the SAICAR synthetase family. {ECO:0000305}.
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DR EMBL; Z95151; CAB08411.1; -; Genomic_DNA.
DR EMBL; AL583924; CAC31183.1; -; Genomic_DNA.
DR PIR; G87187; G87187.
DR RefSeq; NP_302456.1; NC_002677.1.
DR RefSeq; WP_010908776.1; NC_002677.1.
DR AlphaFoldDB; O08361; -.
DR SMR; O08361; -.
DR STRING; 272631.ML2227; -.
DR EnsemblBacteria; CAC31183; CAC31183; CAC31183.
DR KEGG; mle:ML2227; -.
DR PATRIC; fig|272631.5.peg.4227; -.
DR Leproma; ML2227; -.
DR eggNOG; COG0152; Bacteria.
DR HOGENOM; CLU_045637_0_0_11; -.
DR OMA; TKFEFGF; -.
DR UniPathway; UPA00074; UER00131.
DR Proteomes; UP000000806; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004639; F:phosphoribosylaminoimidazolesuccinocarboxamide synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniRule.
DR HAMAP; MF_00137; SAICAR_synth; 1.
DR InterPro; IPR028923; SAICAR_synt/ADE2_N.
DR InterPro; IPR001636; SAICAR_synth.
DR InterPro; IPR018236; SAICAR_synthetase_CS.
DR Pfam; PF01259; SAICAR_synt; 1.
DR TIGRFAMs; TIGR00081; purC; 1.
DR PROSITE; PS01057; SAICAR_SYNTHETASE_1; 1.
DR PROSITE; PS01058; SAICAR_SYNTHETASE_2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Ligase; Nucleotide-binding; Purine biosynthesis;
KW Reference proteome.
FT CHAIN 1..297
FT /note="Phosphoribosylaminoimidazole-succinocarboxamide
FT synthase"
FT /id="PRO_0000100842"
SQ SEQUENCE 297 AA; 33163 MW; 6B3E81E6702FA680 CRC64;
MRPALFDYRH LASGKVREIY RIDDEHLLMV ASDRISAFDY VLDSTIPDKG RILTAMSVFF
FSFVDAPNHL AGPPDDPRIP EEVLGRALVV RQLDMLPMEC VARGYLTGSG LLDYQATGKV
CGIPLPPGLV EASRFAAPLF TPAMKAVLGE HDENISFSRM IEMVGVVRAN QLRDRTLQIY
LQAADHALKT GIIIADTKFE FGIDRDGNLL LADEIFTPDS SRYWSVDDYR VGVVQRSFDK
QFVRNWLVSP ESGWVRAGAL SPPSLPDDII EATRLCYVEV YERISGMSFD DWIGPGA
